December 1, 1982Journal of Biological ChemistryOpen Access

The binding of smooth muscle heavy meromyosin to actin in the presence of ATP. Effect of phosphorylation.

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Population

Smooth muscle heavy meromyosin (HMM) from turkey gizzards

Comparison

Phosphorylation of the 20,000-dalton light chains vs Unphosphorylated HMM

Design

Preclinical

Authors

JSJames R. SellersHeart Failure & Transplant EEE EisenbergNational Institutes of Health RARobert AdelsteinHeart Failure / Cardiomyopathy

Discussion

Member takes

Implication

Phosphorylation modulates smooth muscle myosin kinetics beyond actin binding; extends kinetic models in animal systems but leaves open human cardiovascular relevance.

Structured PICO

Population

Smooth muscle heavy meromyosin (HMM) from turkey gizzards

Intervention

Phosphorylation of the 20,000-dalton light chains

Comparator

Unphosphorylated HMM

Outcome

Actin binding constants in the presence of ATPsurrogate

Phosphorylation of smooth muscle myosin regulates actin-myosin interaction at a kinetic step other than the initial binding of HMM to actin, likely phosphate release or a preceding step.

Cite This Study

Sellers et al. (1982) studied this question.

synapsesocial.com/papers/6a76faaee29fd788c9f6f806 https://doi.org/10.1016/s0021-9258(19)45310-6

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Implication

Phosphorylation modulates smooth muscle myosin kinetics beyond actin binding; extends kinetic models in animal systems but leaves open human cardiovascular relevance.